The protein methyltransferase TrSAM inhibits cellulase gene expression by interacting with the negative regulator ACE1 in Trichoderma reesei
文献类型: 外文期刊
作者: Zhu, Zhihua 1 ; Zou, Gen 1 ; Chai, Shunxing 1 ; Xiao, Meili 1 ; Wang, Yinmei 1 ; Wang, Pingping 1 ; Zhou, Zhihua 1 ;
作者机构: 1.Chinese Acad Sci, CAS Ctr Excellence Mol Plant Sci, Inst Plant Physiol & Ecol, CAS Key Lab Synthet Biol, 300 FengLin Rd, Shanghai 200032, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Shanghai Acad Agr Sci, Inst Edible Fungi, Shanghai Key Lab Agr Genet & Breeding, 1000 Jinqi Rd, Shanghai 201403, Peoples R China
期刊名称:COMMUNICATIONS BIOLOGY ( 影响因子:5.9; 五年影响因子:6.3 )
ISSN:
年卷期: 2024 年 7 卷 1 期
页码:
收录情况: SCI
摘要: Protein methylation is a commonly posttranslational modification of transcriptional regulators to fine-tune protein function, however, whether this regulation strategy participates in the regulation of lignocellulase synthesis and secretion in Trichoderma reesei remains unexplored. Here, a putative protein methyltransferase (TrSAM) is screened from a T. reesei mutant with the ability to express heterologous beta-glucosidase efficiently even under glucose repression. The deletion of its encoding gene trsam causes a significant increase of cellulase activities in all tested T. reesei strains, including transformants of expressing heterologous genes using cbh1 promotor. Further investigation confirms that TrSAM interacts with the cellulase negative regulator ACE1 via its amino acid residue Arg(383), which causes a decrease in the ACE1-DNA binding affinity. The enzyme activity of a T. reesei strain harboring ACE1(R383Q) increases by 85.8%, whereas that of the strains with trsam or ace1 deletion increases by more than 100%. By contrast, the strain with ACE1(R383K) shows no difference to the parent strain. Taken together, our results demonstrate that TrSAM plays an important role in regulating the expression of cellulase and heterologous proteins initiated by cbh1 promotor through interacting with ACE1(R383). Elimination and mutation of TrSAM and its downstream ACE1 alleviate the carbon catabolite repression (CCR) in expressing cellulase and heterologous protein in varying degrees. This provides a new solution for the exquisite modification of T. reesei chassis.
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